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Distinct regulation of autophagic activity by Atg14L and Rubicon associated with Beclin 1–phosphatidylinositol-3-kinase complex
Open accessAbstract
Beclin 1, a mammalian autophagy protein that has been implicated in development, tumour suppression, neurodegeneration and cell death, exists in a complex with Vps34, the class III phosphatidylinositol-3-kinase (PI(3)K) that mediates multiple vesicle-trafficking processes including endocytosis and autophagy. However, the precise role of the Beclin 1-Vps34 complex in autophagy regulation remains to be elucidated. Combining mouse genetics and biochemistry, we have identified a large in vivo Beclin 1 complex containing the known proteins Vps34, p150/Vps15 and UVRAG, as well as two newly identified proteins, Atg14L (yeast Atg14-like) and Rubicon (RUN domain and cysteine-rich domain containing, Beclin 1-interacting protein). Characterization of the new proteins revealed that Atg14L enhances Vps34 lipid kinase activity and upregulates autophagy, whereas Rubicon reduces Vps34 activity and downregulates autophagy. We show that Beclin 1 and Atg14L synergistically promote the formation of double-membraned organelles that are associated with Atg5 and Atg12, whereas forced expression of Rubicon results in aberrant late endosomal/lysosomal structures and impaired autophagosome maturation. We hypothesize that by forming distinct protein complexes, Beclin 1 and its binding proteins orchestrate the precise function of the class III PI(3)K in regulating autophagy at multiple steps.
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In the citing paper
“Yeast Atg14 is the autophagy-specific subunit of the Vps34 complex I, 404 and a human homolog, named ATG14 (ATG14L/BARKOR), has been identified.[405][406][407][408]”
From Guidelines for the use and interpretation of assays for monitoring autophagy (2012) · cites this paper as [406]
Experimental — accuracy not yet measuredIn the citing paper
“the class III phosphoinositide 3-kinase (PI3K) complex regulates vesicle nucleation and phagophore formation”
From Autophagy in kidney homeostasis and disease (2020) · cites this paper as [10]
In the citing paper
“Defects in induction, maturation, or lysosomal clearance impair protein degradation (Zhong et al. 2009), (Pickford et al. 2008), (Ravikumar et al. 2005), (Webb et al. 2004), (Iwata et al. 2005), (Kimura et al. 2008), (Wong and Cuervo 2010), (Lee et al. 2010), and is assessable via LC3-II turnover or p62 degradation (Mizushima et al. 2010), (Ju et al. 2010), (Klionsky et al. 2008b), (Tanida et al.”
From TMEM55B downregulation promotes neurodegeneration in Alzheimer’s disease models (2026) · cites this paper as Zhong et al. 2009
In the citing paper
“Detection of endogenous phospho-ATG16L1 [823] has been demonstrated as a novel method to monitor autophagy induction.”
From Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition) 1 (2021) · cites this paper as [823]
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LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing.
Kabeya, Y., Mizushima, N., Ueno, T., Yamamoto, A., Kirisako, T., Noda, T., Kominami, E., Ohsumi, Y., & Yoshimori, T. (2000) · The EMBO Journal · doi:10.1093/emboj/19.21.5720 · Cited by 6,605
Pankiv, S., Clausen, T. H., Lamark, T., Brech, A., Bruun, J.-A., Outzen, H., Øvervatn, A., Bjørkøy, G., & Johansen, T. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702824200 · Cited by 4,578
Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice
Hara, T., Nakamura, K., Matsui, M., Yamamoto, A., Nakahara, Y., Suzuki-Migishima, R., Yokoyama, M., Mishima, K., Saito, I., Okano, H., et al. (2006) · Nature · doi:10.1038/nature04724 · Cited by 3,882
Loss of autophagy in the central nervous system causes neurodegeneration in mice
Komatsu, M., Waguri, S., Chiba, T., Murata, S., Iwata, J.-I., Tanida, I., Ueno, T., Koike, M., Uchiyama, Y., Kominami, E., et al. (2006) · Nature · doi:10.1038/nature04723 · Cited by 3,500
Induction of autophagy and inhibition of tumorigenesis by beclin 1
Liang, X. H., Jackson, S., Seaman, M., Brown, K., Kempkes, B., Hibshoosh, H., & Levine, B. (1999) · Nature · doi:10.1038/45257 · Cited by 3,347
Promotion of tumorigenesis by heterozygous disruption of the beclin 1 autophagy gene
Qu, X., Yu, J., Bhagat, G., Furuya, N., Hibshoosh, H., Troxel, A., Rosen, J., Eskelinen, E.-L., Mizushima, N., Ohsumi, Y., et al. (2003) · Journal of Clinical Investigation · doi:10.1172/jci20039 · Cited by 2,311
A ubiquitin-like system mediates protein lipidation
Ichimura, Y., Kirisako, T., Takao, T., Satomi, Y., Shimonishi, Y., Ishihara, N., Mizushima, N., Tanida, I., Kominami, E., Ohsumi, M., et al. (2000) · Nature · doi:10.1038/35044114 · Cited by 2,139
Homeostatic levels of p62 control cytoplasmic inclusion body formation in autophagy-deficient mice.
Komatsu, M., Waguri, S., Koike, M., Sou, Y.-S., Ueno, T., Hara, T., Mizushima, N., Iwata, J.-I., Ezaki, J., Murata, S., et al. (2007) · Cell · doi:10.1016/j.cell.2007.10.035 · Cited by 2,124
Self-citationYue, Z., Jin, S., Yang, C., Levine, A. J., & Heintz, N. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2436255100 · Cited by 2,116
Self-citationLC3, GABARAP and GATE16 localize to autophagosomal membrane depending on form-II formation
Kabeya, Y., Mizushima, N., Yamamoto, A., Oshitani-Okamoto, S., Ohsumi, Y., & Yoshimori, T. (2004) · Journal of Cell Science · doi:10.1242/jcs.01131 · Cited by 1,394
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The class IA phosphatidylinositol 3-kinase p110-β subunit is a positive regulator of autophagy
Dou, Z., Chattopadhyay, M., Pan, J.-A., Guerriero, J. L., Jiang, Y.-P., Ballou, L. M., Yue, Z., Lin, R. Z., & Zong, W. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.201006056 · Cited by 93
Self-citationMitophagy in the Pathogenesis of Liver Diseases
Ke, P. (2020) · Cells · doi:10.3390/cells9040831 · Cited by 91
McLeod, I. X., Zhou, X., Li, Q.-J., Wang, F., & He, Y.-W. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1100710 · Cited by 91
The pleiotropic roles of autophagy regulators in melanogenesis
Ho, H., & Ganesan, A. K. (2011) · Pigment Cell & Melanoma Research · doi:10.1111/j.1755-148x.2011.00889.x · Cited by 88
Abrahamsen, H., Stenmark, H., & Platta, H. W. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.04.046 · Cited by 92
Beclin 1 Complex in Autophagy and Alzheimer Disease
Jaeger, P. A., & Wyss‐Coray, T. (2010) · Archives of Neurology · doi:10.1001/archneurol.2010.258 · Cited by 93
Autophagy stimulation as a promising approach in treatment of neurodegenerative diseases
Pierzynowska, K., Gaffke, L., Cyske, Z., Puchalski, M., Rintz, E., Bartkowski, M., Osiadły, M., Pierzynowski, M., Mantej, J., Piotrowska, E., et al. (2018) · Metabolic Brain Disease · doi:10.1007/s11011-018-0214-6 · Cited by 93
Chen, Y.-H., Huang, T.-Y., Lin, Y.-T., Lin, S., Li, W.-H., Hsiao, H.-J., Yan, R.-L., Tang, H.-W., Shen, Z., Chen, G., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-21715-1 · Cited by 91
He, S., Zhao, Z., Yang, Y., O’Connell, D., Zhang, X., Oh, S., Ma, B., Lee, J.-H., Zhang, T., Varghese, B. A., et al. (2015) · Nature Communications · doi:10.1038/ncomms8839 · Cited by 92
Young, L. N., Cho, K., Lawrence, R., Zoncu, R., & Hurley, J. H. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1603650113 · Cited by 89
Conformational flexibility of BECN1: Essential to its key role in autophagy and beyond
Yang, M., Glover, K., Su, M., & Sinha, S. C. (2016) · Protein Science · doi:10.1002/pro.2984 · Cited by 88
Targeting of early endosomes by autophagy facilitates EGFR recycling and signalling
Dudley-Fraser, J., Simpson, J. E., Fontana, R., Kishi‐Itakura, C., Ktistakis, N. T., & Gammoh, N. (2019) · EMBO Reports · doi:10.15252/embr.201947734 · Cited by 88
Liuzzi, J. P., Guo, L., Yoo, C., & Stewart, T. S.-J. (2014) · BioMetals · doi:10.1007/s10534-014-9773-0 · Cited by 88
Promoting Autophagic Clearance: Viable Therapeutic Targets in Alzheimer's Disease
Friedman, L. G., Qureshi, Y. H., & Yu, W. H. (2014) · Neurotherapeutics · doi:10.1007/s13311-014-0320-z · Cited by 89
Omegasomes: PI3P platforms that manufacture autophagosomes
Roberts, R. L., & Ktistakis, N. T. (2013) · Essays in Biochemistry · doi:10.1042/bse0550017 · Cited by 98
ULK1 O-GlcNAcylation Is Crucial for Activating VPS34 via ATG14L during Autophagy Initiation
Pyo, K. E., Kim, C. R., Lee, M., Kim, J.-S., Kim, K. I., & Baek, S. H. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.11.042 · Cited by 86
Defective autophagy in spastizin mutated patients with hereditary spastic paraparesis type 15
Vantaggiato, C., Crimella, C., Airoldi, G., Polishchuk, R., Bonato, S., Brighina, E., Scarlato, M., Musumeci, O., Toscano, A., Martinuzzi, A., et al. (2013) · Brain · doi:10.1093/brain/awt227 · Cited by 89
WIPI1 Coordinates Melanogenic Gene Transcription and Melanosome Formation via TORC1 Inhibition
Ho, H., Kapadia, R., Al-Tahan, S., Ahmad, S., & Ganesan, A. K. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.200543 · Cited by 90
ULK1 targets Beclin-1 in autophagy
Nazarko, V. Y., & Zhong, Q. (2013) · Nature Cell Biology · doi:10.1038/ncb2797 · Cited by 89
Liang, Q., Chang, B., Brulois, K., Castro, K., Min, C., Rodgers, M. A., Shi, M., Ge, J., Feng, P., Oh, B., et al. (2013) · Journal of Virology · doi:10.1128/jvi.01898-13 · Cited by 89
Wang, Y.-T., Liu, T.-Y., Shen, C.-H., Lin, S., Hung, C.-C., Hsu, L.-C., & Chen, G. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.110354 · Cited by 85
Autophagy in Pulmonary Diseases
Nakahira, K., Pabon Porras, M. A., & Choi, A. M. K. (2016) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.201512-2468so · Cited by 78
Brier, L. W., Ge, L., Stjepanović, G., Thelen, A. M., Hurley, J. H., & Schekman, R. W. (2019) · Molecular Biology of the Cell · doi:10.1091/mbc.e18-11-0743 · Cited by 87
Zhi, X., & Zhong, Q. (2015) · F1000Prime Reports · doi:10.12703/p7-18 · Cited by 83
mTOR independent regulation of macroautophagy by Leucine Rich Repeat Kinase 2 via Beclin-1
Manzoni, C., Mamais, A., Roosen, D. A., Dihanich, S., Soutar, M. P. M., Plun‐Favreau, H., Bandopadhyay, R., Hardy, J., Tooze, S. A., Cookson, M., et al. (2016) · Scientific Reports · doi:10.1038/srep35106 · Cited by 89
Molecular machinery of macroautophagy and its deregulation in diseases
Wong, A. S. L., Cheung, Z. H., & Ip, N. Y. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.07.005 · Cited by 95
Phospholipase D2 Mediates Survival Signaling through Direct Regulation of Akt in Glioblastoma Cells
Bruntz, R. C., Taylor, H. E., Lindsley, C. W., & Brown, H. A. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.532978 · Cited by 84
Chen, J., Chen, M. X., Fogo, A. B., Harris, R. C., & Chen, J.-K. (2013) · Journal of the American Society of Nephrology · doi:10.1681/asn.2012010101 · Cited by 82
The role of ESCRT proteins in fusion events involving lysosomes, endosomes and autophagosomes
Metcalf, D. J., & Isaacs, A. M. (2010) · Biochemical Society Transactions · doi:10.1042/bst0381469 · Cited by 90
Bidirectional Control of Autophagy by BECN1 BARA Domain Dynamics
Chang, C., Young, L. N., Morris, K. L., von Bülow, S., Schöneberg, J., Yamamoto‐Imoto, H., Oe, Y., Yamamoto, K., Nakamura, S., Stjepanović, G., et al. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.10.035 · Cited by 83
Small-molecule G-quadruplex stabilizers reveal a novel pathway of autophagy regulation in neurons
Moruno-Manchon, J. F., Lejault, P., Wang, Y., McCauley, B. S., Honarpisheh, P., Morales‐Scheihing, D., Singh, S. S., Dang, W., Kim, N., Urayama, A., et al. (2020) · eLife · doi:10.7554/elife.52283 · Cited by 84
Nguyen, T. T. P., Kim, D. Y., Lee, Y.-G., Lee, Y.-S., Truong, X. T., Lee, J., Song, D., Kwon, T. K., Park, S., Jung, C. H., et al. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.06.003 · Cited by 86
The Importance of Autophagy Regulation in Breast Cancer Development and Treatment
Zarzynska, J. M. (2014) · BioMed Research International · doi:10.1155/2014/710345 · Cited by 82
Banerjee, P., Basu, A., Wegiel, B., Otterbein, L. E., Mizumura, K., Gasser, M., Waaga-Gasser, A. M., Choi, A. M. K., & Pal, S. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.393140 · Cited by 81
Divergent roles of BECN1 in LC3 lipidation and autophagosomal function
He, R., Peng, J., Yuan, P., Xu, F. Z., & Wei, W. (2015) · Autophagy · doi:10.1080/15548627.2015.1034404 · Cited by 81
Redox Regulation in Amyotrophic Lateral Sclerosis
Parakh, S., Spencer, D. M. S., Halloran, M. A., Soo, K. Y., & Atkin, J. D. (2013) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2013/408681 · Cited by 85
The Evolving, Multifaceted Roles of Autophagy in Cancer
Liu, J., & Debnath, J. (2016) · Advances in cancer research · doi:10.1016/bs.acr.2016.01.005 · Cited by 82
Zhong, Y., Morris, D. H., Jin, L., Patel, M. S., Karunakaran, S. K., Fu, Y.-J., Matuszak, E. A., Weiss, H. L., Chait, B. T., & Wang, Q. J. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.561134 · Cited by 79
Self-citationAutophagy modulation: a potential therapeutic approach in cardiac hypertrophy
Wang, X., & Cui, T. (2017) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00145.2017 · Cited by 79
Hassanpour, M., Rezabakhsh, A., Pezeshkian, M., Rahbarghazi, R., & Nouri, M. (2018) · Stem Cell Research & Therapy · doi:10.1186/s13287-018-1060-5 · Cited by 80
A time to reap, a time to sow: Mitophagy and biogenesis in cardiac pathophysiology
Andres, A. M., Stotland, A., Queliconi, B. B., & Gottlieb, R. A. (2015) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2014.10.003 · Cited by 78
Autophagy dysregulation in Danon disease
Nascimbeni, A. C., Fanin, M., Angelini, C. I., & Sandri, M. (2017) · Cell Death and Disease · doi:10.1038/cddis.2016.475 · Cited by 80
Phosphoinositide 3-kinases as accelerators and brakes of autophagy
O’Farrell, F., Rusten, T. E., & Stenmark, H. (2013) · FEBS Journal · doi:10.1111/febs.12486 · Cited by 81
Cytoplasmic sphingosine-1-phosphate pathway modulates neuronal autophagy
Moruno-Manchon, J. F., Uzor, N.-E., Dabaghian, Y. A., Furr-Stimming, E. E., Finkbeiner, S. M., & Tsvetkov, A. S. (2015) · Scientific Reports · doi:10.1038/srep15213 · Cited by 77
Autophagy-active beclin-1 correlates with favourable clinical outcome in non-Hodgkin lymphomas
Nicotra, G., Mercalli, F., Peracchio, C., Castino, R., Follo, C., Valente, G., & Isidoro, C. (2010) · Modern Pathology · doi:10.1038/modpathol.2010.80 · Cited by 81
PAQR3 controls autophagy by integrating AMPK signaling to enhance ATG14L‐associated PI3K activity
Xu, D., Wang, Z., Wang, C.-Y., Zhang, D., Wan, H., Zhao, Z., Gu, J., Zhang, Y., Li, Z., Man, K., et al. (2016) · The EMBO Journal · doi:10.15252/embj.201592864 · Cited by 79
Wan, J., Weiss, E., Ben Mkaddem, S., Mabire, M., Choinier, P.-M., Picq, O., Thibault-Sogorb, T., Hegde, P., Pishvaie, D., Bens, M., et al. (2020) · Science Translational Medicine · doi:10.1126/scitranslmed.aaw8523 · Cited by 77
Where do they come from? Insights into autophagosome formation
Hamasaki, M., & Yoshimori, T. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.02.061 · Cited by 79
Sherwood, R. K., & Roy, C. R. (2016) · Annual Review of Microbiology · doi:10.1146/annurev-micro-102215-095557 · Cited by 81
Noda, N. N., Kobayashi, T., Adachi, W., Fujioka, Y., Ohsumi, Y., & Inagaki, F. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.348250 · Cited by 78
Chang, T., Wei, P., Makondi, P. T., Chen, W.-T., Huang, C., & Chang, Y. (2019) · PLoS ONE · doi:10.1371/journal.pone.0210274 · Cited by 81
Molecular Mechanism of Autophagosome–Lysosome Fusion in Mammalian Cells
Ke, P. (2024) · Cells · doi:10.3390/cells13060500 · Cited by 82
Autophagy—from molecular mechanisms to clinical relevance
Lippai, M., & Szatmári, Z. (2016) · Cell Biology and Toxicology · doi:10.1007/s10565-016-9374-5 · Cited by 80
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Debnath, J. (2011) · Journal of Mammary Gland Biology and Neoplasia · doi:10.1007/s10911-011-9223-3 · Cited by 78
FXR-dependent Rubicon induction impairs autophagy in models of human cholestasis
Panzitt, K., Jungwirth, E., Krones, E., Lee, J. M., Pollheimer, M. J., Thallinger, G., Kolb-Lenz, D., Xiao, R., Thorell, A., Trauner, M., et al. (2020) · Journal of Hepatology · doi:10.1016/j.jhep.2020.01.014 · Cited by 77
Macrophage Autophagy in Atherosclerosis
Maiuri, M. C., Grassia, G., Platt, A. M., Carnuccio, R., Ialenti, A., & Maffia, P. (2013) · Mediators of Inflammation · doi:10.1155/2013/584715 · Cited by 72
GSK-3β promotes cell survival by modulating Bif-1-dependent autophagy and cell death
Yang, J., Takahashi, Y., Cheng, E., Liu, J., Terranova, P. F., Zhao, B., Thrasher, J. B., Wang, H., & Li, B. (2010) · Journal of Cell Science · doi:10.1242/jcs.060475 · Cited by 74
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Ma, B., Cao, W., Li, W., Gao, C., Qi, Z., Zhao, Y. G., Du, J., Xue, H., Peng, J., Wen, J., et al. (2014) · Cell Research · doi:10.1038/cr.2014.84 · Cited by 70
Redox regulation of autophagy in skeletal muscle
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Stroupe, C. (2018) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2018.00129 · Cited by 72
Down-regulation of Beclin1 promotes direct cardiac reprogramming
Wang, L., Ma, H., Huang, P., Xie, Y., Near, D., Wang, H., Xu, J., Yang, Y., Xu, Y., Garbutt, T. A., et al. (2020) · Science Translational Medicine · doi:10.1126/scitranslmed.aay7856 · Cited by 70
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Vehlow, A., Klapproth, E., Jin, S., Hannen, R., Hauswald, M., Bartsch, J. W., Nimsky, C., Temme, A., Leitinger, B., & Cordes, N. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.02.096 · Cited by 70
A fine-tuning mechanism underlying self-control for autophagy: deSUMOylation of BECN1 by SENP3
Liu, K., Guo, C. W., Lao, Y., Yang, J., Chen, F., Zhao, Y., Yang, Y. A., Yang, J., & Yi, J. (2019) · Autophagy · doi:10.1080/15548627.2019.1647944 · Cited by 72
Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)
Klionsky, D. J., Abdelmohsen, K., Abe, A., Abedin, J., Abeliovich, H., Acevedo‐Arozena, A., Adachi, H., Adams, C. M., Adams, P. D., Adeli, K., et al. (2016) · Kölner Universitäts PublikationsServer (Universität zu Köln) · doi:10.5167/uzh-131237 · Cited by 69
The role of autophagy in steroid necrosis of the femoral head: a comprehensive research review
Luo, P., Gao, F., Han, J., Sun, W. M., & Li, Z. (2018) · International Orthopaedics · doi:10.1007/s00264-018-3994-8 · Cited by 68
Zhang, X., Wang, L., Ireland, S., Ahat, E., Li, J., Bekier, M. E., Zhang, Z., & Wang, Y. (2019) · Autophagy · doi:10.1080/15548627.2019.1596480 · Cited by 67
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Dinkins, C., Pilli, M., & Kehrl, J. H. (2014) · Immunology and Cell Biology · doi:10.1038/icb.2014.88 · Cited by 70
Signaling and other functions of lipids in autophagy: a review
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Gong, J.-S., & Kim, G. J. (2014) · Daehan saengsik uihak hoeji/Clinical and experimental reproductive medicine · doi:10.5653/cerm.2014.41.3.97 · Cited by 69
Iranpour, M., Moghadam, A. R., Yazdi, M., Ande, S. R., Alizadeh, J., Wiecheć, E., Lindsay, L. R., DREBOT, M. A., Coombs, K. M., & Ghavami, S. (2016) · Expert Reviews in Molecular Medicine · doi:10.1017/erm.2015.19 · Cited by 70
Sun, Y., Cai, Y., & Zang, Q. S. (2019) · Cells · doi:10.3390/cells8020141 · Cited by 69
Liang, S., Wu, Y.-S., Li, D.-Y., Tang, J., & Liu, H. (2022) · Aging and Disease · doi:10.14336/ad.2021.1027 · Cited by 68
Lipid droplet and early autophagosomal membrane targeting of Atg2A and Atg14L in human tumor cells
Pfisterer, S. G., Bakula, D., Frickey, T., Cezanne, A., Brigger, D., Tschan, M. P., Robenek, H., & Proikas‐Cezanne, T. (2014) · Journal of Lipid Research · doi:10.1194/jlr.m046359 · Cited by 67
Emerging roles of autophagy in metabolism and metabolic disorders
Rocchi, A., & He, C. (2015) · Frontiers in Biology · doi:10.1007/s11515-015-1354-2 · Cited by 66
Wu, S., He, Y., Qiu, X., Yang, W., Liu, W., Li, X., Li, Y., Shen, H., Wang, R., Yue, Z., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1721173115 · Cited by 66
Self-citationReggiori, F., Komatsu, M., Finley, K. D., & Simonsen, A. (2012) · International Journal of Cell Biology · doi:10.1155/2012/156272 · Cited by 68
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Wang, S., Xia, P., Rehm, M., & Fan, Z. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1829-3 · Cited by 66
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Xu, F., Gu, J., & Qin, Z. (2012) · Neuroscience Bulletin · doi:10.1007/s12264-012-1268-9 · Cited by 66
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Bologna, C., Buonincontri, R., Serra, S., Vaisitti, T., Audrito, V., Brusa, D., Pagnani, A., Coscia, M., D'Arena, G. F., Mereu, E., et al. (2015) · Journal of Clinical Investigation · doi:10.1172/jci83013 · Cited by 68
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Sil, P., Muse, G. W., & Martinez, J. (2017) · Current Opinion in Immunology · doi:10.1016/j.coi.2017.10.004 · Cited by 68
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Wong, E. S. P., Bejarano, E., Rakshit, M., Lee, K., Hanson, H. H., Zaarur, N., Phillips, G. R., Sherman, M. Y., & Cuervo, A. M. (2012) · Nature Communications · doi:10.1038/ncomms2244 · Cited by 68
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Orsi, A., Polson, H. E. J., & Tooze, S. A. (2009) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2009.11.013 · Cited by 68
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Magné, J., & Green, D. R. (2022) · Science Advances · doi:10.1126/sciadv.abo5600 · Cited by 64
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Cavignac, Y., & Esclatine, A. (2010) · Viruses · doi:10.3390/v2010314 · Cited by 67
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Liu, J., Wang, H., Gu, J., Deng, T., Yuan, Z.-C., Hu, B., Xu, Y., Yan, Y., Zan, J., Liao, M., et al. (2017) · Autophagy · doi:10.1080/15548627.2017.1280220 · Cited by 66
Self-citationPavlinov, I., Salkovski, M., & Aldrich, L. N. (2020) · Journal of the American Chemical Society · doi:10.1021/jacs.9b12705 · Cited by 63
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Li, Y., Zhao, Y., Hu, J. N., Xiao, J., Qu, L., Wang, Z., Ma, D., & Chen, Y. (2012) · Autophagy · doi:10.4161/auto.22742 · Cited by 66
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Kim, S. H., & Kim, H. (2019) · Marine Drugs · doi:10.3390/md17100546 · Cited by 64
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Liang, W., & Gustafsson, Å. B. (2020) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2020.00018 · Cited by 65
Sahni, S., Merlot, A. M., Krishan, S., Jansson, P. J., & Richardson, D. R. (2014) · Journal of Clinical Pathology · doi:10.1136/jclinpath-2014-202356 · Cited by 65
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Morris, D. H., Yip, C. K., Shi, Y., Chait, B. T., & Wang, Q. J. (2015) · Frontiers in Biology · doi:10.1007/s11515-015-1374-y · Cited by 66
Self-citationAutophagy, reactive oxygen species and the fate of mammalian cells
Szumiel, I. (2010) · Free Radical Research · doi:10.3109/10715762.2010.525233 · Cited by 61
Nemazanyy, I., Montagnac, G., Russell, R. C., Morzyglod, L., Burnol, A.-F., Guan, K.-L., Pende, M., & Panasyuk, G. (2015) · Nature Communications · doi:10.1038/ncomms9283 · Cited by 64
Metadata
- Authors
- Zhong, Y., Wang, Q. J., Li, X., Yan, Y., Backer, J. M., Chait, B. T., Heintz, N., & Yue, Z.
- Affiliations
- Howard Hughes Medical Institute (US)
- Rockefeller University (US)
- Icahn School of Medicine at Mount Sinai (US)
- Albert Einstein College of Medicine (US)
- Corresponding author
- Yue, Zhenyu
- ORCID
- Venue
- Nature Cell Biology
- Published
- 2009-03-08
- Volume
- 11
- Issue
- 4
- Pages
- 468-476
- ISSN
- 1465-7392 (ISSN-L)
- 1476-4679
- PMC
- PMC2664389
- OpenAlex
- W1983831622
- Cited by
- 1,005
- References
- 35
- Citations by year
- 2026: 29 · 2025: 43 · 2024: 38 · 2023: 48 · 2022: 63 · 2021: 62 · 2020: 69 · 2019: 51 · 2018: 57 · 2017: 58 · 2016: 72 · 2015: 56 · 2014: 64 · 2013: 77 · 2012: 64
- FWCI
- 49.02
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- U.S. Public Health Service (RNS055683A)
- National Institute of Neurological Disorders and Stroke (R21NS055683, R01NS060123)
- National Center for Research Resources (RR00862, P41RR000862, RR 022220, U54RR022220)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Calcium signaling and nucleotide metabolism
- Keywords
- autophagy regulation, Beclin-1, ATG14L, Rubicon, Vps34, class III phosphatidylinositol 3-kinase, UVRAG, autophagosome maturation, late endosomes, lysosomes, ATG5, ATG12, lipid kinase activity
- MeSH terms
- Beclin-1, Amino Acid Sequence, Animals, Autophagy, Cell Membrane, HeLa Cells, Humans, Lysosomes, Molecular Sequence Data, Protein Binding, Proteins, Endosomes, Phosphatidylinositol Phosphates, Phosphatidylinositol 3-Kinases, NIH 3T3 Cells, Adaptor Proteins, Signal Transducing, Green Fluorescent Proteins, Apoptosis Regulatory Proteins, Mice
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